Comparison of the paralogous transcription factors AraR and XlnR in Aspergillus oryzae

Curr Genet. 2018 Dec;64(6):1245-1260. doi: 10.1007/s00294-018-0837-5. Epub 2018 Apr 13.

Abstract

The paralogous transcription factors AraR and XlnR in Aspergillus regulate genes that are involved in degradation of cellulose and hemicellulose and catabolism of pentose. AraR and XlnR target the same genes for pentose catabolism but target different genes encoding enzymes for polysaccharide degradation. To uncover the relationship between these paralogous transcription factors, we examined their contribution to regulation of the PCP genes and compared their preferred recognition sequences. Both AraR and XlnR are involved in induction of all the pentose catabolic genes in A. oryzae except larA encoding L-arabinose reductase, which was regulated by AraR but not by XlnR. DNA-binding studies revealed that the recognition sequences of AraR and XlnR also differ only slightly; AraR prefers CGGDTAAW, while XlnR prefers CGGNTAAW. All the pentose catabolic genes possess at least one recognition site to which both AraR and XlnR can bind. Cooperative binding by the factors was not observed. Instead, they competed to bind to the shared sites. XlnR bound to the recognition sites mentioned above as a monomer, but bound to the sequence TTAGSCTAA on the xylanase promoters as a dimer. Consequently, AraR and XlnR have significantly similar, but not the same, DNA-binding properties. Such a slight difference in these paralogous transcription factors may lead to complex outputs in enzyme production depending on the concentrations of coexisting inducer molecules in the natural environment.

Keywords: AraR; Aspergillus oryzae; Pentose catabolism; XlnR.

Publication types

  • Comparative Study

MeSH terms

  • Aspergillus oryzae / chemistry
  • Aspergillus oryzae / genetics
  • Aspergillus oryzae / metabolism*
  • Fungal Proteins / chemistry
  • Fungal Proteins / genetics
  • Fungal Proteins / metabolism*
  • Gene Expression Regulation, Fungal / physiology*
  • Pentose Phosphate Pathway / physiology*
  • Protein Multimerization / physiology*
  • Response Elements*
  • Trans-Activators / chemistry
  • Trans-Activators / genetics
  • Trans-Activators / metabolism*

Substances

  • Fungal Proteins
  • Trans-Activators
  • XlnR protein, Aspergillus